1n5d

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CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASECRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE

Structural highlights

1n5d is a 1 chain structure with sequence from Sus scrofa. This structure supersedes the now removed PDB entry 1hu4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBR1_PIG NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione (By similarity).[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Tanaka M, Ohno S, Adachi S, Nakajin S, Shinoda M, Nagahama Y. Pig testicular 20 beta-hydroxysteroid dehydrogenase exhibits carbonyl reductase-like structure and activity. cDNA cloning of pig testicular 20 beta-hydroxysteroid dehydrogenase. J Biol Chem. 1992 Jul 5;267(19):13451-5. PMID:1377683

1n5d, resolution 2.30Å

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OCA